H-Lys-Lys-Glu-Thr-Leu-Gln-Phe-Arg-OH combines basic, acidic, hydrophobic, and aromatic residues that generate a diverse interaction landscape. Researchers study its hydrogen-bond tendencies and folding in aqueous systems. Charge distribution influences binding and structural adaptability. Applications include motif mapping, peptide engineering, and biophysical evaluation.
CAT No: R2633
CAS No:146877-90-9
Synonyms/Alias:CMX-8933;EX-A9705;HY-P10506;CS-1102380;146877-90-9;
H-Lys-Lys-Glu-Thr-Leu-Gln-Phe-Arg-OH is a synthetic peptide composed of eight amino acid residues arranged in a specific sequence, representing a versatile tool for modern biochemical and molecular research. As a linear peptide featuring both hydrophilic and hydrophobic residues, it offers a balanced physicochemical profile suitable for a range of experimental applications. The presence of charged, polar, and nonpolar side chains within the sequence enables diverse interactions with proteins, enzymes, and cellular components, making it valuable for studies involving peptide-protein binding, structural biology, and functional analysis. Its synthetic origin ensures batch-to-batch consistency, which is crucial for reproducible scientific investigations in peptide chemistry and related disciplines.
Peptide-protein interaction studies: The sequence of H-Lys-Lys-Glu-Thr-Leu-Gln-Phe-Arg-OH is particularly well-suited for probing specific binding events between peptides and protein targets. Researchers can employ this octapeptide as a model ligand to evaluate the affinity and specificity of protein receptors, enzymes, or antibodies. Its combination of basic, acidic, and neutral residues allows for the exploration of electrostatic, hydrogen bonding, and hydrophobic interactions, providing insights into the molecular determinants of biomolecular recognition and complex formation.
Enzyme substrate and inhibitor research: Due to its defined amino acid composition, this peptide serves as a valuable substrate or competitive inhibitor in enzymatic assays. Proteases, kinases, or peptidases can be tested for their ability to cleave or modify the sequence, enabling detailed kinetic analyses and mechanism-of-action studies. Such applications are essential for characterizing enzyme specificity, mapping cleavage sites, and screening for novel modulators within drug discovery or basic enzymology research.
Peptide structure-function analysis: The distinct arrangement of residues in H-Lys-Lys-Glu-Thr-Leu-Gln-Phe-Arg-OH facilitates investigations into how sequence variations influence secondary structure, stability, and biological activity. Through spectroscopic, calorimetric, or computational methods, scientists can dissect the conformational tendencies of the peptide, assess its folding properties, and correlate structural features with functional outcomes. These studies contribute to a deeper understanding of peptide design principles and the development of bioactive analogs.
Cell signaling and receptor engagement assays: As a synthetic peptide, this sequence can be applied in cell-based experiments to mimic or disrupt endogenous signaling pathways. By introducing the peptide into cultured cells or tissue preparations, researchers can evaluate its capacity to activate, inhibit, or modulate receptor-mediated processes. Such assays are instrumental in elucidating the roles of short peptide motifs in cellular communication, signal transduction, and downstream biological responses.
Analytical method calibration and validation: The well-defined nature of H-Lys-Lys-Glu-Thr-Leu-Gln-Phe-Arg-OH makes it an excellent standard for calibrating and validating analytical techniques such as high-performance liquid chromatography (HPLC), mass spectrometry, and capillary electrophoresis. Laboratories can utilize the peptide to assess instrument performance, optimize separation protocols, and ensure the accuracy of peptide quantification in complex mixtures. This application supports rigorous quality control and method development in proteomics, peptide synthesis, and related analytical fields.
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